The immune response depends on the binding of opsonized antigens to cellular Fc receptors and the following initiation of cellular effector functions of the immune system. The crystal structures of a soluble Fcgamma receptor, an Fc fragment, and their complex explain a wealth of functional data of the system. They also provide a rationale for the modulation of effector activities by changes of the domain arrangement of the Fc fragment caused by altered glycosylation. Myelin oligodendrocyte glycoprotein (MOG) is a major autoantigen in multiple sclerosis. The crystal structures of MOG and its complex with a specific autoantibody provide a basis for new diagnostic and therapeutic strategies against the pathogenic autoantibody response to MOG.These molecular structures offer multiple ways to interfere with the cellular immune response in autoimmune diseases:

a) by small molecules disrupting the Fc receptor-Fc contact;b) by antibodies directed against the contact area;c) by soluble Fc receptors as antagonists;d) by mimeticsof the MOG epitop.

Animal experiments following strategies b) and c) have been successfully completed for three model autoimmune diseases, SLE, arthritis, and EAE.

A company SUPPREMOL has been founded to pursue these strategies on a commercial basis and has obtained licences from the Max-Planck-Gesellschaft. Financing has been secured by a partnership with Z-cube, the Zambon Group (Milano, Italy ) corporate venture capital arm.